Structure of BT_3984, a member of the SusD/RagB family of nutrient-binding molecules
Journal Article
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· Acta Crystallographica. Section F
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- Joint Center for Structural Genomics, http://www.jcsg.org (United States); Sanford–Burnham Medical Research Inst., La Jolla, CA (United States). Program on Bioinformatics and Systems Biology; DOE/OSTI
- Joint Center for Structural Genomics, http://www.jcsg.org (United States); SLAC National Accelerator Lab., Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL)
- Joint Center for Structural Genomics, http://www.jcsg.org (United States); Genomics Institute of the Novartis Research Foundation, San Diego, CA (United States). Protein Sciences Dept.
- Joint Center for Structural Genomics, http://www.jcsg.org (United States); Univ. of California, San Diego, La Jolla, CA (United States). Center for Research in Biological Systems
- Joint Center for Structural Genomics, http://www.jcsg.org (United States); The Scripps Research Inst., La Jolla, CA (United States). Dept. of Molecular Biology
- Joint Center for Structural Genomics, http://www.jcsg.org (United States); Sanford–Burnham Medical Research Inst., La Jolla, CA (United States). Program on Bioinformatics and Systems Biology; Univ. of California, San Diego, La Jolla, CA (United States). Center for Research in Biological Systems
- Joint Center for Structural Genomics, http://www.jcsg.org (United States); Sanford–Burnham Medical Research Inst., La Jolla, CA (United States). Program on Bioinformatics and Systems Biology
- Joint Center for Structural Genomics, http://www.jcsg.org (United States); SLAC National Accelerator Lab., Menlo Park, CA (United States). Photon Science
- Joint Center for Structural Genomics, http://www.jcsg.org (United States); Genomics Institute of the Novartis Research Foundation, San Diego, CA (United States). Protein Sciences Dept.; The Scripps Research Inst., La Jolla, CA (United States). Dept. of Molecular Biology
The crystal structure of the Bacteroides thetaiotaomicron protein BT_3984 was determined to a resolution of 1.7 Å and was the first structure to be determined from the extensive SusD family of polysaccharide-binding proteins. SusD is an essential component of the sus operon that defines the paradigm for glycan utilization in dominant members of the human gut microbiota. Structural analysis of BT_3984 revealed an N-terminal region containing several tetratricopeptide repeats (TPRs), while the signature C-terminal region is less structured and contains extensive loop regions. Sequence and structure analysis of BT_3984 suggests the presence of binding interfaces for other proteins from the polysaccharide-utilization complex.
- Research Organization:
- SLAC National Accelerator Laboratory, Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL)
- Sponsoring Organization:
- USDOE Office of Science (SC), Biological and Environmental Research (BER); National Institutes of Health (NIH); National Institute of General Medical Sciences (NIGMS); National Center for Research Resources (NCRR); USDOE Office of Science (SC), Basic Energy Sciences (BES)
- Grant/Contract Number:
- AC02-76SF00515
- OSTI ID:
- 1625804
- Alternate ID(s):
- OSTI ID: 22367349
- Journal Information:
- Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: 10 Vol. 66; ISSN ACSFCL; ISSN 1744-3091
- Publisher:
- International Union of CrystallographyCopyright Statement
- Country of Publication:
- United States
- Language:
- English
Structure of RagB, a major immunodominant outer-membrane surface receptor antigen of Porphyromonas gingivalis
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journal | November 2015 |
Polysaccharide Utilization Loci: Fueling Microbial Communities
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journal | January 2017 |
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